Abstract
Proteasomes reach their mature active state via a complex cascade of folding, assembly and processing events. The Rhodococcus proteasome offers a means to dissect the assembly pathway and to characterize intermediates; its four subunits (alpha1, alpha2, beta1, beta2) assemble efficiently in vitro with any combination of alpha and beta. Assembly studies with wild-type and N-terminally truncated beta-subunits in conjunction with refolding studies allowed to define the role of the propeptide which is two-fold: It supports the initial folding of the beta-subunits and it promotes the maturation of the holoproteasomes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cloning, Molecular
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Cysteine Endopeptidases / biosynthesis*
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Cysteine Endopeptidases / chemistry
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Cysteine Endopeptidases / ultrastructure
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Enzyme Precursors / chemistry
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Kinetics
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Macromolecular Substances
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Microscopy, Electron
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Models, Molecular
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Multienzyme Complexes / biosynthesis*
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Multienzyme Complexes / chemistry
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Multienzyme Complexes / ultrastructure
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Polymerase Chain Reaction
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Proteasome Endopeptidase Complex
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Protein Conformation*
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Protein Denaturation
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Protein Folding*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Rhodococcus / enzymology*
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Sequence Tagged Sites
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Substrate Specificity
Substances
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Enzyme Precursors
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Macromolecular Substances
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Multienzyme Complexes
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Recombinant Proteins
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex